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PubMed2006

Intersite structural rearrangement of the blue copper site induced by substrate binding: spectroscopic studies of a copper-containing nitrite reductase from Alcaligenes xylosoxidans NCIMB 11015.

A copper-containing nitrite reductase from Alcaligenes xylosoxidans NCIMB 11015 has its own unique blue or type 1 copper protein resonance Raman spectrum in the usual Cu-S(Cys) stretching region, nu(Cu-S(Cys)), with a pair of strong peaks at 412 and 420 cm(-1) and a weak peak at 364 cm(-1). The predominantly nu(Cu-S(Cys)) Raman bands at 412, 420, and 364 cm(-1) of the type 1 copper site all shifted to higher frequencies upon binding of nitrite to the type 2 copper site, and the resonance Raman difference spectra progressively intensified with the increments of nitrite ion concentration. Positive support for substrate binding to the type 2 copper is provided by the nu(Cu-S(Cys)) bands in the resonance Raman spectrum of a type 2 copper-depleted enzyme, which is insensitive to the presence of NO2-. The shift to higher frequency of the Raman bands of the type 1 copper center with the addition of nitrite ions suggests a stronger Cu-S(Cys) interaction in the substrate-bound A. xylosoxidans nitrite reductase.

Alcaligenes↗

PubMed2003

Radiation-induced enhancement of nitrite reducing activity of cytochrome c.

Commercial cytochrome c (Cyt c) was irradiated with Co-60 gamma-rays in the dose range of up to 3.0 kGy to investigate the enhancement of the nitrite reducing activity of Cyt c. The optimum irradiation dose to induce nitrite reducing activity for 30 muM Cyt c solution was 1.0 kGy under an O(2) atmosphere. The nitrite reducing activity of Cyt c irradiated at this dose was approximately 45-fold that of unirradiated Cyt c and ca. 1.2-fold that of nitrite reductase. The irradiation treatment resulted in unfolding of the peptide chain, exposure of the heme group, oxidation of methionine to methionine sulfoxide, dissociation of the sixth ligand (Met), and occurrence of autoxidation in Cyt c. Sepharose-immobilized irradiated Cyt c had a similar activity to that in solution. The resin retained the activity after five uses even after 1 year of storage. The irradiated Cyt c will be able to be used as a substitute for nitrite reductase.

Circular Dichroism↗

PubMed2002

Inhibition of lipid peroxidation in synaptosomes and liposomes by nitrates and nitrites.

NO is produced endogenously from arginine by the action of NO synthase, and exogenously by nitrovasodilators, including organic nitrates and nitrites. NO has been proposed as a cytotoxic and cytoprotective agent. There is strong evidence that NO acts as an apparent antioxidant in inhibiting lipid peroxidation, via chain termination, and interestingly lipid nitrates and nitrites have been proposed to be products of this chain termination. Both pro- and antioxidant mechanisms may be drawn for nitrates and nitrites; therefore, their effects on lipid peroxidation were measured in two systems, using tocopherol, thiol, and an NO donor for comparison: (1) rat cerebrocortical synaptosomes with Fe(II)-induced lipid peroxidation measured by thiobarbituric acid reactive substances (TBARS), and (2) phospholipid liposomes with an azo-initiator induction system, quantified by a fluorescent probe of peroxide formation. In contrast to the classical nitrate nitroglycerin, novel nitrates which release NO on reaction with thiols and two novel nitrates which spontaneously generate NO in aqueous solution inhibited lipid peroxidation. i-Amyl nitrite inhibited lipid peroxidation, and its properties were further studied with ESR spectroscopy. The data show that classical nitrites and novel nitrates are not prooxidants, but inhibit lipid peroxidation.

Amyl Nitrite↗

PubMed2003

Nitrite-induced nitration pathways of retinoic acid, 5,6-epoxyretinoic acid, and their esters under mildly acidic conditions: toward a reappraisal of retinoids as scavengers of reactive nitrogen species.

All trans retinoic acid (1), a cancer chemopreventive agent and a pluripotent morphogen, was found to react efficiently with nitrite ions in a biphasic system consisting of CH(2)Cl(2)/0.1 M phosphate buffer (pH 3) 1:1 v/v to give a complex mixture of nitration products. Repeated TLC fractionation of the reaction mixtures after methylation allowed isolation of the main products, which could be identified as the 12-nitro derivatives 3a,b and the decarboxylated 12,14-dinitro and 5,6-epoxy-14-nitro derivatives 4 and 5a by spectral analysis. Use of (15)NO(2)(-) followed by extensive 2D NMR analysis, including (1)H,(15)N heteronuclear multiple bond correlation experiments, allowed identification of nitronitrate derivatives as additional constituents of the mixture. Under similar conditions, 1 methyl ester gave mainly 3a,b. 5,6-Epoxyretinoic acid (2) reacted smoothly with acidic nitrite to give mainly 5a and its isomer 5b whereas its methyl ester afforded 14-nitro derivatives 9a,b as chief products. The observed patterns of reactivity along with mechanistic experiments would suggest that nitrite-induced nitration of 1 proceeds through complex reaction pathways set in motion by attack of NO(2) to the 12- and 14-positions. Separate experiments showed that 1 can inhibit nitrite-induced N-nitrosation of 2,3-diaminonaphthalene at pH values of 4 and 5.5, as well as decomposition of caffeic acid under similar conditions. Overall, these results provide the first detailed insight into the reaction behavior of a retinoid toward reactive nitrogen species and shed light on previously overlooked nitrite scavenging properties of 1 of potential relevance to the mechanism of its antiinflammatory, antimutagenic, and cancer chemopreventive action.

Antineoplastic Agents↗

PubMed1997

Inhibition of denitrification activity but not of mRNA induction in Paracoccus denitrificans by nitrite at a suboptimal pH.

The influence of pH on the denitrification activity of a continuous culture of Paracoccus denitrificans was studied in relation to the presence of nitrite. After a transition from aerobic to anaerobic conditions at the suboptimal pH of 6.8, P. denitrificans was not able to build up a functional denitrification pathway. Nitrite accumulated in the medium as the predominant denitrification product. Although the nitrite reductase gene was induced properly, the enzyme could not be detected at sufficient amounts in the culture. These observations was somehow inhibited, or once synthesized nitrite reductase was inactivated, possibly by the high concentrations of nitrous acid (HNO2). Interestingly, when a P. denitrificans culture which was grown to steady-state under anaerobic conditions was then exposed to suboptimal pHs, cells exhibited a reduced overall denitrification activity, but neither nitrite nor any other denitrification intermediate accumulated.

Anaerobiosis↗

PubMed1982

Purification and properties of the assimilatory nitrite reductase from barley Hordeum vulgare leaves.

The assimilatory nitrite reductase (ferredoxin: nitrite oxidoreductase, EC 1.7.7.1) from barley (Hordeum vulgare L.) leaves has been purified over 1500-fold with a recovery of 30% and a specific activity of 84 mumol of nitrite reduced/min per mg of protein. The purification procedure includes (NH4)2SO4 fractionation, ion-exchange and molecular-sieve chromatographies and, finally, ferredoxin-Sepharose-4B affinity chromatography. The enzyme appears homogeneous by polyacrylamide gel electrophoresis and consists of a single polypeptide chain with an Mr of 61 000. The absorption spectrum of the pure enzyme was typical of a haem-containing protein. The enzyme showed low thermostability and was specific for ferredoxin (Km 0.4 microM), although reduced Methyl Viologen (Km 120 microM) was also effective. The same Km value for nitrite (250 microM) was obtained with both electron carriers. Cyanide acted as a powerful pure competitive inhibitor of enzyme with respect to nitrite (Ki 40 microM). Thiol-blocking agents also caused considerable inhibition, but only the ferredoxin-driven activity was significantly inhibited by sulphite and hydroxylamine.

Catalysis↗

PubMed1987

Tumorigenicity study in Syrian hamsters fed areca nut together with nitrite.

In order to evaluate the effect of concurrent administration of areca nut and sodium nitrite, a long-term feeding study was conducted with 120 Syrian hamsters. The animals were divided into four treatment groups, each consisting of 15 males and 15 females, and received 2 g/kg diet of sodium nitrite (group I), 20 g/kg diet of powdered areca nut (group II), 2 g/kg diet of sodium nitrite plus 20 g/kg diet of areca nut (group III) or powdered diet only (group IV) throughout their lifetime. Urine samples from all groups were analysed for N-nitrosonipecotic acid (NNIP), a major urinary metabolite of areca-nut-derived nitrosamines. NNIP was only detected in the urine of hamsters fed nitrite plus areca nut (concentration: 1.9 +/- 0.9 ng/ml urine), indicating that areca nut alkaloids underwent in vivo nitrosation to form areca-nut-specific nitrosamines. The total tumour response was not significantly elevated in groups II and III. Hamsters of group III had a markedly, but also insignificantly higher frequency of malignant tumours than those of the other groups, with a statistically significant increase in malignant lymphomas in the males. Although limited by the low number of animals per group, these results indicate that exposure to nitrite together with areca nut constituents appears to enhance the risk of developing malignancies.

Animals↗

PubMed1985

Isolation, characterization and complementation analysis of nirB mutants of Escherichia coli deficient only in NADH-dependent nitrite reductase activity.

Mutants have been isolated which lack NADH-dependent nitrite reductase activity but retain NADPH-dependent sulphite reductase and formate hydrogenlyase activities. These NirB- strains synthesize cytochrome c552 and grow normally on anaerobic glycerol-fumarate plates. The defects map in a gene, nirB, which is extremely close to cysG, the gene order being crp, nirB, cysG, aroB. Complementation studies established that nirB+ and cysG+ can be expressed independently. The data strongly suggest that nirB is the structural gene for the 88 kDal NADH-dependent nitrite oxidoreductase apoprotein (EC 1.6.6.4). The nirB gene is apparently defective in the previously described nirD mutant, LCB82. The nirH mutant, LCB197, was unable to use formate as electron donor for nitrite reduction, but NADH-dependent nitrite reductase was extremely active in this strain and a normal content of cytochrome c552 was detected. Strains carrying a nirE, nirF or nirG mutation gave normal rates of nitrite reduction by glucose, formate or NADH.

Chromosome Mapping↗

PubMed2005

The pathogen Neisseria meningitidis requires oxygen, but supplements growth by denitrification. Nitrite, nitric oxide and oxygen control respiratory flux at genetic and metabolic levels.

The human pathogen Neisseria meningitidis is the major causative agent of bacterial meningitis. The organism is usually treated as a strict aerobe and is cultured under fully aerobic conditions in the laboratory. We demonstrate here that although N. meningitidis fails to grow under strictly anaerobic conditions, under oxygen limitation the bacterium expresses a denitrification pathway (reduction of nitrite to nitrous oxide via nitric oxide) and that this pathway supplements growth. The expression of the gene aniA, which encodes nitrite reductase, is regulated by oxygen depletion and nitrite availability via transcriptional regulator FNR and two-component sensor-regulator NarQ/NarP respectively. Completion of the two-step denitrification pathway requires nitric oxide (NO) reduction, which proceeds after NO has accumulated during batch growth under oxygen-limited conditions. During periods of NO accumulation both nitrite and NO reduction are observed aerobically, indicating N. meningitidis can act as an aerobic denitrifier. However, under steady-state conditions in which NO is maintained at a low concentration, oxygen respiration is favoured over denitrification. NO inhibits oxidase activity in N. meningitidis with an apparent Ki NO = 380 nM measured in intact cells. The high respiratory flux to nitrite after microaerobic growth and the finding that accumulation of the denitrification intermediate NO inhibits oxygen respiration support the view that denitrification is a pathway of major importance in N. meningitidis.

Adult↗

PubMed1997

Diversity of oxygen and N-oxide regulation of nitrite reductases in denitrifying bacteria.

We examined alpha, beta and gamma Proteobacteria with Cu and heme-type dissimilatory nitrite reductases for patterns of nir regulation. Six of seven strains expressed nitrite reductase under aerobic growth conditions. In only one strain, G-179, was it stringently regulated by O2. Growth with NO-3 or NO-2 enhanced nitrite reductase production in four of seven strains under anaerobic growth conditions, but in only one strain, Pseudomonas aeruginosa PA01, under aerobic conditions. In this strain the nitrite reductase production was primarily regulated by an anr gene when grown under anaerobic conditions, but when grown under aerobic conditions it was regulated by both an anr gene and nitrogen oxide. Constitutive production of nitrite reductase was a common phenomenon rather than the exception among denitrifiers from the environment, which helps explain the prevalence of denitrifying enzymes in aerobic soils.

Aerobiosis↗

PubMed1979

Effect of processing variables on the outgrowth of Clostridium sporogenes PA 3679 spores in comminuted meat cured with sorbic acid and sodium nitrite.

The effects of the initial pH and a "short pump" on the outgrowth of Clostridium sporogenes PA 3679 spores in comminuted cured pork were studied. Fresh ground pork was cured with salt, sugar, phosphate, ascorbate, and varying amounts of sodium nitrite and sorbic acid. The product was comminuted and inoculated with 1,000 spores of C. sporogenes per g. The meat was stuffed into 1-ounce (ca. 28.4-g) aluminum tubes, cooked to 58.5 degrees C, cooled, and incubated at 27 degrees C to observe for swells. Product cured with 0.2% sorbic acid in combination with 40 ppm sodium nitrite (40 microgram/g) had better clostridium inhibition than did product cured with 120 ppm nitrite within a pH range of 5.0 to 6.7. The sorbic acid-40 ppm nitrite combination also gave better clostridial protection than did the 120 ppm nitrite alone when reduced amounts of curing ingredients were present.

Animals↗

PubMed1984

Anaerobic growth of Neisseria gonorrhoeae coupled to nitrite reduction.

A total of 204 Neisseria gonorrhoeae strains, including 39 penicillinase-producing strains, representing 64 distinct auxotype and serovar classes were tested for their ability to grow anaerobically with nitrite as a terminal electron acceptor. All strains grew anaerobically with subtoxic concentrations of nitrite, and all penicillinase-producing strains produced beta-lactamase when grown anaerobically. Nitrite reductase was produced constitutively under aerobic conditions in the absence of nitrite, and cytochrome oxidase was produced constitutively under anaerobic conditions. Strains could not grow anaerobically with sulfite as a terminal electron acceptor. Strain NRL 905 grew anaerobically in broth medium containing nitrite at a rate comparable to its growth rate under aerobic conditions. The feasibility and significance of in vivo anaerobic growth of N. gonorrhoeae is discussed.

Anaerobiosis↗

PubMed1975

Enzymatic and non-enzymatic reduction of nitrite by extracts of Neurospora crassa.

Two activites causing nitrite disappearance are found in extracts of Neurospora; one, inducible by nitrate or nitrite and present only in nitrite-utilizing strains, catalyze the stoichiometric reduction of nitrite to ammonia; the other, present in all strains under all conditions, causes the disappearance of nitrite to something other than ammonia. The latter activity has a molecular weight of about 600 and may contain an oligopeptide, a metal, and an SH group(s). It has no known physiological function.

Ammonia↗

PubMed2005

Enzymatic function of hemoglobin as a nitrite reductase that produces NO under allosteric control.

Hypoxic vasodilation is a fundamental, highly conserved physiological response that requires oxygen and/or pH sensing coupled to vasodilation. While this process was first characterized more than 80 years ago, the precise identity and mechanism of the oxygen sensor and mediators of vasodilation remain uncertain. In support of a possible role for hemoglobin (Hb) as a sensor and effector of hypoxic vasodilation, here we show biochemical evidence that Hb exhibits enzymatic behavior as a nitrite reductase, with maximal NO generation rates occurring near the oxy-to-deoxy (R-to-T) allosteric structural transition of the protein. The observed rate of nitrite reduction by Hb deviates from second-order kinetics, and sigmoidal reaction progress is determined by a balance between 2 opposing chemistries of the heme in the R (oxygenated conformation) and T (deoxygenated conformation) allosteric quaternary structures of the Hb tetramer--the greater reductive potential of deoxyheme in the R state tetramer and the number of unligated deoxyheme sites necessary for nitrite binding, which are more plentiful in the T state tetramer. These opposing chemistries result in a maximal nitrite reduction rate when Hb is 40-60% saturated with oxygen (near the Hb P50), an apparent ideal set point for hypoxia-responsive NO generation. These data suggest that the oxygen sensor for hypoxic vasodilation is determined by Hb oxygen saturation and quaternary structure and that the nitrite reductase activity of Hb generates NO gas under allosteric and pH control.

Allosteric Regulation↗

PubMed1991

Denitrification by the fungus Fusarium oxysporum and involvement of cytochrome P-450 in the respiratory nitrite reduction.

From conditions for production in Fusarium oxysporum of the unique nitrate/nitrite-inducible cytochrome P-450, tentatively called P-450dNIR, it was expected that the fungus is capable of metabolizing nitrate dissimilatively. Here we report that F. oxysporum exhibits a distinct denitrifying ability which results in the anaerobic evolution of nitrous oxide (N2O) from nitrate or nitrite. Comparison of the cell growth during denitrification indicated that the dissimilatory reduction of nitrate to nitrite is an energetically favorable process in F. oxysporum; however, further reduction of nitrite to N2O might be energy-exhausting and may function as a detoxification mechanism. A potent nitrite reductase activity to form N2O could be reconstituted by combination of the cell-free extract prepared from the denitrifying cells and an NADH-phenadinemethosulfate-dependent reducing system. The activity was strongly inhibited by carbon monoxide, cyanide, oxygen (O2), and the antibody against P-450dNIR. The results, along with those concerning inducing conditions of P-450dNIR, were highly indicative that the cytochrome is involved in the denitrifying nitrite reduction. This work has thus presented not only the first demonstration that a eukaryote exhibits a marked denitrifying ability, but also the first instance of a cytochrome P-450 that is involved in a reducing reaction with a distinct physiological significance against a hydrophilic, inorganic substrate.

Cytochrome P-450 Enzyme System↗

PubMed1989

[Effect of the combined action of sodium nitrite and fenitrothion on certain biochemical parameters in rat blood].

The aim of the study was explaining of the combined action of low doses of sodium nitrite and fenitrothion on certain biochemical parameters in rat blood. The experiment was carried out on male adult Wistar rats. The animals were divided into 4 experimental groups: group I receiving 10 mg/kg of sodium nitrite, group II--2.5 mg/kg of fenitrothion (Owadofos), group III received a mixture of both these doses, group IV served as control. The preparations were given intragastrically through a tube for 90 days. After that time 2,3-diphosphoglyceric acid, vitamin E, SH groups in protein and non-protein compounds in erythrocytes, methaemoglobin and basic haematological parameters, as well as the activity of glucose-6-phosphate dehydrogenase, superoxide dismutase and choline esterase were determined. Sodium nitrite decreased the activity of glucose-6-phosphate dehydrogenase and vitamin E, with an increase of the activity of superoxide dismutase and protein SH groups and methaemoglobin level. fenitrothion caused similar changes as sodium nitrite and decreased the activity of choline esterase and the level of 2,3-diphosphoglyceric acid. No synergistic action of these compounds was noted. The level of non-protein SH groups was decreased. It seems that determination of the level of non-protein sulphohydryl groups may be one of the indicators of poisoning with sodium nitrite combined with phenitrotione.

Animals↗

PubMedDate not supplied

Acute effects of some volatile nitrites on motor performance and lethality in mice.

Mice were examined for effects on lethality and motor performance on an inverted screen test following inhalation exposure to isoamyl, n-butyl and isobutyl nitrite. All three nitrites produced concentration-related effects on both measures, with EC50s for motor performance only about one-half of the LC50s for lethality. Isoamyl and isobutyl nitrite were equally potent on both lethality and motor performance measures, whereas n-butyl nitrite was significantly more potent than isoamyl and isobutyl for lethality. Slope estimates of the concentration-effect curves for lethality were significantly greater than those of the motor performance measure. The steepness of the concentration-effect curves and low LC50/EC50 ratios relative to abused organic solvents suggest that behaviorally active concentrations of volatile nitrites may put users at risk to other health consequences.

Aerosols↗

PubMed1987

[Oxidation by nitrite of azurin and cytochrome c-551 from Pseudomonas aeruginosa].

The nitrite oxidizes reduced azurin and cytochrome c-551 from Pseudomonas aeruginosa. The effects of pH, ionic strength and concentrations of nitrite, EDTA and the protein on the oxidation were investigated. The results obtained indicate that nitrite interacts not only with the terminal electron carrier of the nitrite reducing chain (nitrite reductase, cytochrome cd1) but also with the intermediate electron carrier components of the chain (azurin and cytochrome c-551).

Azurin↗